A double-headed trypsin inhibitor(MCI-1)was isolated and purified from the seeds of Momordica charantia Linn.Cucurbitaceae,by using the trypsin-sepharose-4B affinity chroma- tography and CM-Sephadex-C50 ion exchange c...A double-headed trypsin inhibitor(MCI-1)was isolated and purified from the seeds of Momordica charantia Linn.Cucurbitaceae,by using the trypsin-sepharose-4B affinity chroma- tography and CM-Sephadex-C50 ion exchange chromatography.It is composed of 77 amino acid residues:Asp_8 Thr_1 Ser_4 Glu_8 Pro_2 Gly_6 Ala_4 Cys_(14) Val_2 Met_4 Ile_8 Leu_1 Phe_1 His_3 Lys_ Arg_7. The amino acid sequence of MCI-1 was determined by sequencing the cyanogen bromide,tryptic and staphylococcus aureus V8 proteolytic peptides,then aligned by overlapped sequences.The result shows that MCI-1 contains 7 pairs of disulfide bonds,its sequence showed the high homology with those of “Bowman-Birk”inhibitors.About 50% trypsin inhibitory activity still remained after MCI-1 was cleavaged with cyanogen bromide.展开更多
文摘A double-headed trypsin inhibitor(MCI-1)was isolated and purified from the seeds of Momordica charantia Linn.Cucurbitaceae,by using the trypsin-sepharose-4B affinity chroma- tography and CM-Sephadex-C50 ion exchange chromatography.It is composed of 77 amino acid residues:Asp_8 Thr_1 Ser_4 Glu_8 Pro_2 Gly_6 Ala_4 Cys_(14) Val_2 Met_4 Ile_8 Leu_1 Phe_1 His_3 Lys_ Arg_7. The amino acid sequence of MCI-1 was determined by sequencing the cyanogen bromide,tryptic and staphylococcus aureus V8 proteolytic peptides,then aligned by overlapped sequences.The result shows that MCI-1 contains 7 pairs of disulfide bonds,its sequence showed the high homology with those of “Bowman-Birk”inhibitors.About 50% trypsin inhibitory activity still remained after MCI-1 was cleavaged with cyanogen bromide.
